Component
The hydroxylated proline residues of HIF-1alpha
The hydroxylated proline residues of HIF-1alpha. Species, exposure and limitations are retained in each linked claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
Where it participates (unsigned role)
Silencing PHD2 alone was sufficient to stabilise and activate HIF-1alpha in normoxia in every human cell type investigated, while silencing PHD1 or PHD3 had no effect on HIF-1alpha stability, making PHD2 the critical oxygen sensor setting the low steady-state level of HIF-1alpha.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/hbot-research/12912907.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "db0613321b1804356dbb60637bba0616eaaaeab041f63a095ecfcaeac3ec780e", "start_char": 0, "end_char": 1190, "text_sha256": "db0613321b1804356dbb60637bba0616eaaaeab041f63a095ecfcaeac3ec780e"}
- experimental_model
- Short interfering RNA silencing of each HIF prolyl-hydroxylase in human cells
- exposure
- PHD1, PHD2 and PHD3 silencing in normoxia and after brief hypoxia
- limitations
- A silencing study assigning distinct roles. It establishes which isoform sets the resting level, not the oxygen concentration at which each acts.
- nutrient_topic
- Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
- organism
- Human cells
- plain_language
- One enzyme is the thermostat: it destroys the low-oxygen signal whenever oxygen is present.
- primary_references
- [hbot-p12912907] HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. (2003). https://pubmed.ncbi.nlm.nih.gov/12912907/ DOI: 10.1093/emboj/cdg392
- tissue_or_cell_type
- Cytosol
Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 933–944
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Short interfering RNA silencing of each HIF prolyl-hydroxylase in human cells · source_derived_draft · unverified_draft
### hbot-phd2-oxygen-sensor Silencing PHD2 alone was sufficient to stabilise and activate HIF-1alpha in normoxia in every human cell type investigated, while silencing PHD1 or PHD3 had no effect on HIF-1alpha stability, making PHD2 the critical oxygen sensor setting the low steady-state level of HIF-1alpha. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: One enzyme is the thermostat: it destroys the low-oxygen signal whenever oxygen is present. organism: Human cells tissue_or_cell_type: Cytosol experimental_model: Short interfering RNA silencing of each HIF prolyl-hydroxylase in human cells limitations: A silencing study assigning distinct roles. It establishes which isoform sets the resting level, not the oxygen concentration at which each acts. exposure: PHD1, PHD2 and PHD3 silencing in normoxia and after brief hypoxia evidence_span: {"source_cache": "artifacts/hbot-research/12912907.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "db0613321b1804356dbb60637bba0616eaaaeab041f63a095ecfcaeac3ec780e", "start_char": 0, "end_char": 1190, "text_sha256": "db0613321b1804356dbb60637bba0616eaaaeab041f63a095ecfcaeac3ec780e"} [hbot-p12912907] HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. (2003). https://pubmed.ncbi.nlm.nih.gov/12912907/ DOI: 10.1093/emboj/cdg392
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.